Modulation of Phosphoprotein Activity by Phosphorylation Targeting Chimeras (PhosTACs)

<i>EGFR</i> Mutations in Lung Cancer: Correlation with Clinical Response to Gefitinib Therapy

Paez, J. G., Jänne, P. A., Lee, J. C., Tracy, S., Greulich, H., Gabriel, S., Herman, P., Kaye, F. J., Lindeman, N., Boggon, T. J., et al. (2004) · Science · doi:10.1126/science.1099314 · Cited by 9,368 · see citing works

Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor

Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 6,535 · see citing works

Acquired Resistance of Lung Adenocarcinomas to Gefitinib or Erlotinib Is Associated with a Second Mutation in the EGFR Kinase Domain

Pao, W., Miller, V. A., Politi, K. A., Riely, G. J., Somwar, R., Zakowski, M. F., Kris, M. G., & Varmus, H. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020073 · Cited by 3,527 · see citing works

Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

Olsen, J. V., Blagoev, B., Gnad, F., Maček, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,484 · see citing works

HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis

Los, G. V., Encell, L. P., McDougall, M. G., Hartzell, D., Karassina, N., Zimprich, C., Wood, M. G., Learish, R., Ohana, R. F., Urh, M., et al. (2008) · ACS Chemical Biology · doi:10.1021/cb800025k · Cited by 2,527 · see citing works

Induced protein degradation: an emerging drug discovery paradigm

Lai, A. C., & Crews, C. M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.211 · Cited by 1,486 · see citing works

Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease

Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317 · see citing works

Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes

Vlastaridis, P., Kyriakidou, P., Chaliotis, A., de Peer, Y. V., Oliver, S. G., & Amoutzias, G. D. (2017) · GigaScience · doi:10.1093/gigascience/giw015 · Cited by 732 · see citing works

S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth

Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731 · see citing works

Bcr-Abl kinase domain mutations, drug resistance, and the road to a cure for chronic myeloid leukemia

O’Hare, T., Eide, C. A., & Deininger, M. W. (2007) · Blood · doi:10.1182/blood-2007-03-066936 · Cited by 634 · see citing works

Tau phosphorylation in neuronal cell function and dysfunction

Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624 · see citing works

Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer

Seshacharyulu, P., Pandey, P., Datta, K., & Batra, S. K. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.02.036 · Cited by 479 · see citing works

Targeted Degradation of Oncogenic KRAS ^G12C by VHL-Recruiting PROTACs

Bond, M. J., Chu, L., Nalawansha, D. A., Li, K., & Crews, C. M. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00411 · Cited by 450 · see citing works

Aberrant FGFR signaling mediates resistance to CDK4/6 inhibitors in ER+ breast cancer

Formisano, L., Lu, Y., Servetto, A., Hanker, A. B., Jansen, V. M., Bauer, J. A., Sudhan, D. R., Zotano, Á. G., Croessmann, S., Guo, Y. P., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09068-2 · Cited by 409 · see citing works

Targeting the C481S ibrutinib-resistance mutation in Bruton’s tyrosine kinase using PROTAC-mediated degradation

Buhimschi, A. D., Armstrong, H. A., Toure, M., Jaime-Figueroa, S., Chen, T. L., Lehman, A. M., Woyach, J. A., Johnson, A. J., Byrd, J. C., & Crews, C. M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00391 · Cited by 394 · see citing works

A walk through tau therapeutic strategies

Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 286 · see citing works

Structure‐Based Design of a Macrocyclic PROTAC

Testa, A., Hughes, S. J., Lucas, X., Wright, J. E., & Ciulli, A. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201914396 · Cited by 251 · see citing works

Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion

Rena, G., Woods, Y. L., Prescott, A. R., Peggie, M., Unterman, T. G., Williams, M. R., & Cohen, P. (2002) · The EMBO Journal · doi:10.1093/emboj/21.9.2263 · Cited by 241 · see citing works

Regulation of FOXO protein stability via ubiquitination and proteasome degradation

Huang, H., & Tindall, D. J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.007 · Cited by 227 · see citing works

Cell Cycle and Beyond: Exploiting New RB1 Controlled Mechanisms for Cancer Therapy

Knudsen, E. S., Pruitt, S. C., Hershberger, P. A., Witkiewicz, A. K., & Goodrich, D. W. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.03.005 · Cited by 185 · see citing works

Selective PP2A enhancement through biased heterotrimer stabilization

Leonard, D., Huang, W., Izadmehr, S., O’Connor, C. M., Wiredja, D. D., Wang, Z., Zaware, N., Chen, Y., Schlatzer, D. M., Kiselar, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.038 · Cited by 176 · see citing works

Assessing Different E3 Ligases for Small Molecule Induced Protein Ubiquitination and Degradation

Ottis, P., Toure, M., Cromm, P. M., Ko, E., Gustafson, J. L., & Crews, C. M. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00485 · Cited by 176 · see citing works

Non-canonical functions of the RB protein in cancer

Dick, F. A., Goodrich, D. W., Sage, J., & Dyson, N. J. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0008-5 · Cited by 169 · see citing works

Akt Phosphorylates and Regulates Pdcd4 Tumor Suppressor Protein

Palamarchuk, A., Efanov, A., Maximov, V., Aqeilan, R. I., Croce, C. M., & Pekarsky, Y. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-3469 · Cited by 151 · see citing works

Heterobifunctional Molecules Induce Dephosphorylation of Kinases–A Proof of Concept Study

Yamazoe, S., Tom, J., Fu, Y., Wu, W., Zeng, L., Sun, C., Liu, Q., Lin, J. M., Lin, K., Fairbrother, W. J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01167 · Cited by 145 · see citing works

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

Lambrecht, C., Haesen, D., Sents, W., Ivanova, E., & Janssens, V. (2013) · Methods in Molecular Biology · doi:10.1007/978-1-62703-562-0_17 · Cited by 140 · see citing works

Protein Phosphatase 2A Reactivates FOXO3a through a Dynamic Interplay with 14-3-3 and AKT

Singh, A. J., Ye, M., Bucur, O., Zhu, S., dos Santos, M. T. M. A., Rabinovitz, I., Wei, W., Gao, D., Hahn, W. C., & Khosravi‐Far, R. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-09-0795 · Cited by 117 · see citing works

Mice lacking phosphatase PP2A subunit PR61/B’δ ( <i>Ppp2r5d</i> ) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3β

Louis, J. V., Martens, E., Borghgraef, P., Lambrecht, C., Sents, W., Longin, S., Zwaenepoel, K., Pijnenborg, R., Landrieu, I., Lippens, G., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018777108 · Cited by 112 · see citing works

Global and site-specific effect of phosphorylation on protein turnover

Wu, C.-D., Ba, Q., Lu, D.-Y., Li, W.-X., Šalovská, B., Hou, P., Mueller, T., Rosenberger, G. A., Gao, E., Di, Y., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.10.025 · Cited by 102 · see citing works

The dynamic nature of the kinome

Graves, L. M., Duncan, J. S., Whittle, M. C., & Johnson, G. L. (2013) · Biochemical Journal · doi:10.1042/bj20121456 · Cited by 91 · see citing works

Phosphoproteomic analysis identifies the tumor suppressor PDCD4 as a RSK substrate negatively regulated by 14-3-3

Galan, J. A., Geraghty, K. M., Lavoie, G., Kanshin, E., Tcherkezian, J., Calabrese, V., Jeschke, G. R., Turk, B. E., Ballif, B. A., Blenis, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405601111 · Cited by 85 · see citing works

A novel dephosphorylation targeting chimera selectively promoting tau removal in tauopathies

Zheng, J., Tian, N., Liu, F., Zhang, Y., Su, J., Gao, Y., Deng, M., Wei, L., Ye, J., Li, H., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00669-2 · Cited by 78 · see citing works

Casein kinase 1α–dependent feedback loop controls autophagy in RAS-driven cancers

Cheong, J. K., Zhang, F., Chua, P. J., Bay, B., Thorburn, A. M., & Virshup, D. M. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78018 · Cited by 64 · see citing works

The Highly Recurrent PP2A Aα-Subunit Mutation P179R Alters Protein Structure and Impairs PP2A Enzyme Function to Promote Endometrial Tumorigenesis

Taylor, S. E., O’Connor, C. M., Wang, Z., Shen, G., Song, H., Léonard, D., Sangodkar, J., Lavasseur, C. M., Avril, S., Waggoner, S. E., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0218 · Cited by 58 · see citing works

The split protein phosphatase system

Bertolotti, A. (2018) · Biochemical Journal · doi:10.1042/bcj20170726 · Cited by 56 · see citing works

Controlling Ser/Thr protein phosphatase PP1 activity and function through interaction with regulatory subunits

Casamayor, A., & Ariño, J. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.06.004 · Cited by 37 · see citing works

Targeted protein degradation: from mechanisms to clinic

Tsai, J. M., Nowak, R. P., Ebert, B. L., & Fischer, E. S. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00729-9 · Cited by 438 · see citing works

Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies

Wu, X., Xu, M., Geng, M., Chen, S., Little, P. J., Xu, S., & Weng, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01439-y · Cited by 290 · see citing works

Proximity-Based Modalities for Biology and Medicine

Liu, X., & Ciulli, A. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00395 · Cited by 205 · see citing works

Targeted Dephosphorylation of Tau by Phosphorylation Targeting Chimeras (PhosTACs) as a Therapeutic Modality

Hu, Z., Chen, P.-H., Li, W., Douglas, T., Hines, J., Liu, Y., & Crews, C. M. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11706 · Cited by 98 · see citing works

DNA-encoded library-enabled discovery of proximity-inducing small molecules

Mason, J. W., Chow, Y. T., Hudson, L., Tutter, A., Michaud, G., Westphal, M. V., Shu, W., Ma, X., Tan, Z. Y., Coley, C. W., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01458-4 · Cited by 83 · see citing works

NDA Submission of Vepdegestrant (ARV-471) to U.S. FDA: The Beginning of a New Era of PROTAC Degraders

Ma, Z., & Zhou, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01818 · Cited by 80 · see citing works

PROTAC Delivery Strategies for Overcoming Physicochemical Properties and Physiological Barriers in Targeted Protein Degradation

Syahputra, E. W., Lee, H., Cho, H. J., Park, H. J., Park, K., & Hwang, D. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17040501 · Cited by 82 · see citing works

Protein Phosphatase 5-Recruiting Chimeras for Accelerating Apoptosis-Signal-Regulated Kinase 1 Dephosphorylation with Antiproliferative Activity

Zhang, Q., Wu, X., Zhang, H., Wu, Q., Fu, M., Hua, L., Zhu, X., Guo, Y., Zhang, L., You, Q., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c10759 · Cited by 72 · see citing works

Targeted Covalent Modification Strategies for Drugging the Undruggable Targets

Tamura, T., Kawano, M., & Hamachi, I. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00745 · Cited by 71 · see citing works

PROTAC 2.0: Expanding the frontiers of targeted protein degradation

Cornu, M., Lemaitre, T., Kieffer, C., & Voisin‐Chiret, A. S. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104376 · Cited by 68 · see citing works

Recent Advances of Degradation Technologies Based on PROTAC Mechanism

Xiao, M., Zhao, J., Wang, Q., Liu, J., & Ma, L. (2022) · Biomolecules · doi:10.3390/biom12091257 · Cited by 66 · see citing works

Targeted protein posttranslational modifications by chemically induced proximity for cancer therapy

Peng, Y., Liu, J., Inuzuka, H., & Wei, W. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104572 · Cited by 66 · see citing works

Beyond Proteolysis-Targeting Chimeric Molecules: Designing Heterobifunctional Molecules Based on Functional Effectors

Hua, L., Zhang, Q., Zhu, X., Wang, R., You, Q., & Wang, L. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00316 · Cited by 66 · see citing works

Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review

Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works

Expanding the horizons of targeted protein degradation: A non-small molecule perspective

Huang, X., Wu, F., Ye, J., Wang, L., Wang, X., Li, X., & He, G. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.01.010 · Cited by 58 · see citing works

Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules

Ma, B., Khan, K. S., Xu, T., Amada, J. X., Guo, Z., Huang, Y., Yan, Y., Lam, H., Cheng, A. S. L., & Ng, W. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c14380 · Cited by 56 · see citing works

Opportunities for Therapeutic Modulation of O-GlcNAc

Cheng, S. S., Mody, A. C., & Woo, C. M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00417 · Cited by 61 · see citing works

Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence

Duran-Frigola, M., Cigler, M., & Winter, G. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11098 · Cited by 50 · see citing works

EGFR targeting PhosTACs as a dual inhibitory approach reveals differential downstream signaling

Hu, Z., Chen, P., Li, W., Krone, M. W., Zheng, S., Saarbach, J., Velasco, I. U., Hines, J. F., Liu, Y., & Crews, C. M. (2024) · Science Advances · doi:10.1126/sciadv.adj7251 · Cited by 46 · see citing works

Proximity-inducing modalities: the past, present, and future

Singh, S., Tian, W., Severance, Z. C., Chaudhary, S. K., Anokhina, V. S., Mondal, B., Pergu, R., Singh, P. R., Dhawa, U., Singha, S., et al. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00943a · Cited by 45 · see citing works

Kinase-targeting small-molecule inhibitors and emerging bifunctional molecules

Goebel, G. L., Qiu, X., & Wu, P. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.04.006 · Cited by 42 · see citing works

Induced proximity-based therapeutic modalities

King, E. A., Meyers, M., & Nomura, D. K. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01316-z · Cited by 42 · see citing works

TAC‐tics for Leveraging Proximity Biology in Drug Discovery

Nalawansha, D. A., Mangano, K., den Besten, W., & Potts, P. R. (2023) · ChemBioChem · doi:10.1002/cbic.202300712 · Cited by 36 · see citing works

Linking ATP and allosteric sites to achieve superadditive binding with bivalent EGFR kinase inhibitors

Wittlinger, F., Ogboo, B. C., Shevchenko, E., Damghani, T., Pham, C. D., Schaeffner, I. K., Oligny, B. T., Chitnis, S. P., Beyett, T. S., Rasch, A., et al. (2024) · Communications Chemistry · doi:10.1038/s42004-024-01108-3 · Cited by 35 · see citing works

Deubiquitinase-Targeting Chimeras (DUBTACs) as a Potential Paradigm-Shifting Drug Discovery Approach

Ma, Z., Zhou, M., Chen, H., Shen, Q., & Zhou, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02975 · Cited by 37 · see citing works

Key Considerations in Targeted Protein Degradation Drug Discovery and Development

Qin, L., Dai, H., & Wang, J. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.934337 · Cited by 34 · see citing works

Protein degraders - from thalidomide to new PROTACs

Ito, T. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad113 · Cited by 33 · see citing works

Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized Proteome

Dionne, U., & Gingras, A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.852911 · Cited by 31 · see citing works

Emerging insights into serine/threonine-specific phosphoprotein phosphatase function and selectivity

Kokot, T., & Köhn, M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259618 · Cited by 30 · see citing works

Metabolism-driven posttranslational modifications and immune regulation: Emerging targets for immunotherapy

Wu, G., Fan, X., Cheng, L., Chen, Z., Yi, Y., Liang, J., Huang, X., Yang, N., Yin, J., Guo, W., et al. (2025) · Science Advances · doi:10.1126/sciadv.adx6489 · Cited by 32 · see citing works

Current strategies for improving limitations of proteolysis targeting chimeras

Pu, C., Wang, S., Liu, L., Feng, Z., Zhang, H., Gong, Q., Sun, Y., Guo, Y., & Li, R. (2022) · Chinese Chemical Letters · doi:10.1016/j.cclet.2022.107927 · Cited by 29 · see citing works

Post-Translational Modifications and Diabetes

Sharma, C., Hamza, A., Boyle, E., Donu, D., & Cen, Y. (2024) · Biomolecules · doi:10.3390/biom14030310 · Cited by 26 · see citing works

An affinity-directed phosphatase, AdPhosphatase, system for targeted protein dephosphorylation

Simpson, L. M., Fulcher, L. J., Sathe, G. J., Brewer, A., Zhao, J., Squair, D. R., Crooks, J., Wightman, M., Wood, N. T., Gourlay, R., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.01.003 · Cited by 25 · see citing works

Roles of posttranslational modifications in lipid metabolism and cancer progression

Feng, T., Zhang, H., Zhou, Y., Zhu, Y., Shi, S., Li, K., Lin, P., & Chen, J. (2024) · Biomarker Research · doi:10.1186/s40364-024-00681-y · Cited by 23 · see citing works

Pooled endogenous protein tagging and recruitment for systematic profiling of protein function

Serebrenik, Y. V., Mani, D. R., Maujean, T., Burslem, G. M., & Shalem, O. (2024) · Cell Genomics · doi:10.1016/j.xgen.2024.100651 · Cited by 22 · see citing works

Targeted dephosphorylation of TFEB promotes its nuclear translocation

Zhao, J., Shpiro, N., Sathe, G. J., Brewer, A., Macartney, T., Wood, N. T., Negoita, F., Sakamoto, K., & Sapkota, G. P. (2024) · iScience · doi:10.1016/j.isci.2024.110432 · Cited by 21 · see citing works

Induced proximity at the cell surface

Till, N. A., Ramanathan, M., & Bertozzi, C. R. (2025) · Nature Biotechnology · doi:10.1038/s41587-025-02592-1 · Cited by 21 · see citing works

Setd2 deficiency promotes gastric tumorigenesis through inhibiting the SIRT1/FOXO pathway

Feng, W., Ma, C., Rao, H., Zhang, W., Liu, C., Xu, Y., Aji, R., Wang, Z., Xu, J., Gao, W., et al. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216470 · Cited by 21 · see citing works

Pooled Tagging and Hydrophobic Targeting of Endogenous Proteins for Unbiased Mapping of Unfolded Protein Responses

Sansbury, S. E., Serebrenik, Y. V., Lapidot, T., Smith, D. G., Burslem, G. M., & Shalem, O. (2023) · Molecular Cell · doi:10.1016/j.molcel.2025.04.002 · Cited by 21 · see citing works

RIPTACs for Precision Cancer Therapy: A Novel Modality with the Inspiration of HLD-0915 as the First Candidate in Clinical Trials

Ma, Z., Zhang, C., Shen, Q., & Zhou, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01250 · Cited by 19 · see citing works

Targeted protein modification as a paradigm shift in drug discovery

Amirian, R., Azadi Badrbani, M., Izadi, Z., Samadian, H., Bahrami, G., Sarvari, S., Abdolmaleki, S., Nabavi, S. M., Derakhshankhah, H., & Jaymand, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115765 · Cited by 18 · see citing works

Allosteric PROTACs: Expanding the Horizon of Targeted Protein Degradation

Frost, A. B., O’Connor, S., & Ciulli, A. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c14840 · Cited by 21 · see citing works

Loss of LCMT1 and biased protein phosphatase 2A heterotrimerization drive prostate cancer progression and therapy resistance

Rasool, R. U., O’Connor, C. M., Das, C. K., Alhusayan, M., Verma, B. K., Islam, S., Frohner, I. E., Deng, Q., Mitchell-Velasquez, E., Sangodkar, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40760-6 · Cited by 17 · see citing works

Discovery and optimisation of a covalent ligand for TRIM25 and its application to targeted protein ubiquitination

McPhie, K. A., Esposito, D., Pettinger, J., Norman, D., Werner, T., Mathieson, T., Bush, J. T., & Rittinger, K. (2025) · Chemical Science · doi:10.1039/d5sc01540e · Cited by 16 · see citing works

Exploring the landscape of post-translational modification in drug discovery

Cao, Y., Yu, T., Zhu, Z., Zhang, Y., Sun, S., Li, N., Gu, C., & Yang, Y. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108749 · Cited by 15 · see citing works

Phosphorylation-Inducing Molecules for Regulating Dynamic Cellular Processes

Pergu, R., Sreekanth, V., Kokkonda, P., Lai, S., Tiwari, P. K., Singh, S., Kawai, J., Singha, S., Tian, W., Thimaradka, V., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c04275 · Cited by 15 · see citing works

Targeted dephosphorylation of SMAD3 as an approach to impede TGF-β signaling

Brewer, A., Zhao, J., Fasimoye, R. Y., Shpiro, N., Macartney, T., Wood, N. T., Wightman, M., Alessi, D. R., & Sapkota, G. P. (2024) · iScience · doi:10.1016/j.isci.2024.110423 · Cited by 14 · see citing works

Nanobody-thioesterase chimeras to specifically target protein palmitoylation

Kuo, C.-W. S., Gök, Ç., Fulton, H., Dickson-Murray, E., Adu, S., Gallen, E., Mary, S., Robertson, A. D., Jordan, F., Dunning, E., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56716-x · Cited by 14 · see citing works

Divergent regulation of KCNQ1/E1 by targeted recruitment of protein kinase A to distinct sites on the channel complex

Zou, X., Shanmugam, S. K., Kanner, S. A., Sampson, K. J., Kass, R. S., & Colecraft, H. M. (2023) · eLife · doi:10.7554/elife.83466 · Cited by 14 · see citing works

Modulating Phosphorylation by Proximity-Inducing Modalities for Cancer Therapy

Zhang, Q., Yu, J., You, Q., & Wang, L. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02624 · Cited by 14 · see citing works

Targeted protein degradation with bifunctional molecules as a novel therapeutic modality for Alzheimer's disease & beyond

Sandhof, C. A., Murray, H. F. B., Silva, M. C., & Haggarty, S. J. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00499 · Cited by 13 · see citing works

Targeting Tau Protein with Proximity Inducing Modulators: A New Frontier to Combat Tauopathies

Uliassi, E., Bolognesi, M. L., & Milelli, A. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00733 · Cited by 13 · see citing works

Targeted Protein Acetylation Through Chemically Induced Proximity

Wang, W., Roy, S. J. S., & Parker, C. G. (2025) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5c00326 · Cited by 12 · see citing works

A General Strategy for the Design and Evaluation of Heterobifunctional Tools: Applications to Protein Localization and Phase Separation

Lackner, R. M., O'Connell, W., Zhang, H., & Chenoweth, D. M. (2022) · ChemBioChem · doi:10.1002/cbic.202200209 · Cited by 12 · see citing works

FDA Approval of the First-Ever PROTAC: Vepdegestrant (ARV-471) Marks a New Era in Targeted Protein Degradation

Kumar, A., Ali, S., Shen, Q., & Zhou, J. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c02076 · Cited by 12 · see citing works

Strategies for Conditional Regulation of Proteins

Nadendla, K., Simpson, G. G., Becher, J. B., Journeaux, T., Cabeza-Cabrerizo, M., & Bernardes, G. J. L. (2023) · JACS Au · doi:10.1021/jacsau.2c00654 · Cited by 11 · see citing works

A protein phosphatase 1 specific phos phatase ta rgeting p eptide (PhosTAP) to identify the PP1 phosphatome

Choy, M. S., Nguyen, H. T., Kumar, G. S., Peti, W., Kettenbach, A. N., & Page, R. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2415383121 · Cited by 11 · see citing works

Advancements in Targeted Quantum Dots Structures for Enhanced Cancer Treatment

Shukla, N., Cárdenas, C. Y., Chanderiya, A., Polozhentsev, O. E., Das, R., Vyas, S., Mukhanova, E., Soldatov, A. V., & Belbekhouche, S. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17111396 · Cited by 10 · see citing works

Chemically modified polysaccharides: A review of structure-activity relationships and mechanisms for enhanced bioactivity

Song, S.-L., Guo, H.-L., Sun, R.-K., Liu, M.-X., Liu, F., Shi, S.-R., Zhang, X.-H., Wei-kun, S., Ji, C., Zou, X., et al. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152192 · Cited by 10 · see citing works

Updates on Tau-Related Drug Targets and Potential Disease-Modifying Therapies for Alzheimer Disease

Djurovic-Topalovic, A., Horgan, N. G., & Fortin, J. S. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.05.020 · Cited by 10 · see citing works

A Functional Assay for Mining Noninhibitory Enzyme Ligands from One Bead One Compound Libraries: Application to E3 Ubiquitin Ligases

Gui, W., Goss, A., & Kodadek, T. J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c07307 · Cited by 10 · see citing works

Discovery of molecular glues that bind FKBP12 and novel targets using DNA-barcoded libraries

Zandi, T. A., Romanowski, M. J., Viscomi, J. S., Tan, Z. Y., Tong, B., Bonazzi, S., Zécri, F. J., Schreiber, S. L., & Michaud, G. A. (2024) · doi:10.1101/2024.12.09.627499 · Cited by 10 · see citing works

Exploitation of Proximity-Mediated Effects in Drug Discovery: An Update of Recent Research Highlights in Perturbing Pathogenic Proteins and Correlated Issues

Zhao, C., Wang, H., Zhan, W., Lv, X., & Ma, X. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00079 · Cited by 9 · see citing works

Recent advances in chemical proteomics for protein profiling and targeted degradation

Liu, P.-K., Wang, Z., & Li, L. (2025) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2025.102605 · Cited by 9 · see citing works

Next‐Generation Proteolysis‐Targeting Chimeras in Precision Oncology: Multifunctional Designs, Emerging Modalities, and Translational Prospects in Targeted Protein Degradation

Nafie, M. S., Diab, M. K., Yassen, A. S. A., Elshamy, A. M., Tohamy, M. R. E., Tawfik, H. O., & Fahmy, S. A. (2025) · Drug Development Research · doi:10.1002/ddr.70192 · Cited by 9 · see citing works

Native mass spectrometry interrogation of complexes formed during targeted protein degradation

Ahmed, I. M. M., & Beveridge, R. (2023) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.9604 · Cited by 9 · see citing works

Natural bioactive compounds and FOXO3a in cancer therapeutics: An update

Manoharan, S., Prajapati, K., & Perumal, E. (2023) · Fitoterapia · doi:10.1016/j.fitote.2023.105807 · Cited by 9 · see citing works

Molecular probes for cellular imaging of post-translational proteoforms

Suraritdechachai, S., Lakkanasirorat, B., & Uttamapinant, C. (2022) · RSC Chemical Biology · doi:10.1039/d1cb00190f · Cited by 9 · see citing works

Harmony of Protein Tags and Chimeric Molecules Empowers Targeted Protein Ubiquitination and Beyond

Lawer, A., Schulz, L. P., Sawyer, R. C., & Liu, X. (2024) · Cells · doi:10.3390/cells13050426 · Cited by 8 · see citing works

Heterobifunctional molecules tackle targeted protein dephosphorylation

Sibley, C. D., & Schneekloth, J. S. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.01.005 · Cited by 8 · see citing works

The rise of targeting chimeras (TACs): next-generation medicines that preempt cellular events

Hollingsworth, S. A., Johnson, S. A., Khakbaz, P., Meng, Y., Mouchlis, V. D., Pierce, O., Prytkova, V. D., Vik, E. S., Weiss, D. R., & Shanmugasundaram, V. (2023) · Medicinal Chemistry Research · doi:10.1007/s00044-023-03104-z · Cited by 8 · see citing works

Deciphering phosphorylation TACtics: Advances in phosphorylation targeting strategies and bifunctional modalities

Ke, D.-T., Zhan, Z., Zhang, W., Hu, Z., & Chen, P. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2025.12.012 · Cited by 7 · see citing works

Engineering brain-penetrant PROTACs: Bridging molecular design and CNS delivery

Li, X., Li, J., Sun, Y., Yao, T., Lu, Y., Liu, S., Li, H., Shi, Y., Chen, L., Zhao, Y., et al. (2026) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2026.115876 · Cited by 7 · see citing works

A heterobifunctional molecule system for targeted protein acetylation in cells

Chen, L., Wang, W., Wozniak, J. M., & Parker, C. G. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.014 · Cited by 7 · see citing works

Rewiring the Fusion Oncoprotein EWSR1::FLI1 in Ewing Sarcoma with Bivalent Small Molecules

Bond, M. J., Golden, R. P., DiGiovanni, G., Howard, B., Sarott, R. C., Karim, B. A., Gourisankar, S. P., Alexe, G., Ross, K. N., Jones, H. M., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c05634 · Cited by 6 · see citing works

Short peptide pharmacophores developed from protein phosphatase-1 disrupting peptides (PDPs)

Fontanillo, M., Trebacz, M., Reinkemeier, C. D., Huerta, D. A., Uhrig, U., Sehr, P. A., & Köhn, M. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116785 · Cited by 6 · see citing works

Methods to characterize and discover molecular degraders in cells

Lin, Z., & Woo, C. M. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00261b · Cited by 6 · see citing works

Generating Surprisingly Powerful Pharmacology from Chemically Induced Protein Interactions

Hinshaw, S. M., Banik, S. M., & Gray, N. S. (2025) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5c00225 · Cited by 5 · see citing works

Reversible control of kinase signaling through chemical-induced dephosphorylation

Sun, Y., Zhou, R., Hu, J., Feng, S., & Hu, Q. (2024) · Communications Biology · doi:10.1038/s42003-024-06771-9 · Cited by 5 · see citing works

To homeostasis and beyond! Recent advances in the medicinal chemistry of heterobifunctional derivatives

Castagna, D., Gourdet, B., Hjerpe, R., MacFaul, P., Novak, A., Révol, G., Rochette, É., & Jordan, A. M. (2024) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2024.07.002 · Cited by 5 · see citing works

Catalytic Protein Inhibitors

Kodadek, T. J. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202316726 · Cited by 5 · see citing works

A phosphorylation-controlled switch confers cell cycle-dependent protein relocalization

Cao, X., Huang, S., Wagner, M. M., Cho, Y., Chiu, D.-C., Wartchow, K. M., Lazarian, A., McIntire, L. B., Smolka, M. B., & Baskin, J. M. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01495-8 · Cited by 5 · see citing works

Design of bifunctional molecules to accelerate post-translational modifications: achievements and challenges

Wang, Y., He, Y., You, Q., & Wang, L. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104194 · Cited by 5 · see citing works

Modulating the phosphorylation status of target proteins through bifunctional molecules

He, Q., Wang, Z., Wang, R., Lu, T., Chen, Y., & Lü, S. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104307 · Cited by 3 · see citing works

From Serendipity to Strategy: Rationalizing Molecular Glue Discovery and Proximity-Induced Pharmacology through Chemical Biology

Gray, J. L., Xiao, Z., Rogga, V. V., Zhang, X., & Tate, E. W. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12299 · Cited by 4 · see citing works

Discovery of molecular glues that bind FKBP12 and structurally distinct targets using DNA-encoded libraries

Zandi, T. A., Romanowski, M. J., Viscomi, J. S., Gunderson, K., Tan, Z. Y., Tong, B., Bonazzi, S., Zécri, F. J., Schreiber, S. L., & Michaud, G. A. (2026) · Nature Communications · doi:10.1038/s41467-026-71512-x · Cited by 4 · see citing works

Dual-action kinase inhibitors influence p38α MAP kinase dephosphorylation

Stadnicki, E. J., Ludewig, H., Kumar, R. P., Wang, X., Qiao, Y., Kern, D., & Bradshaw, N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2415150122 · Cited by 4 · see citing works

A chemical magnet: Approaches to guide precise protein localization

Kumar, S., & Nabet, B. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117672 · Cited by 4 · see citing works

Design and Development of DNA Damage Chemical Inducers of Proximity for Targeted Cancer Therapy

Qiu, T., Lee, Y. T., Dwyer, B. G., Tan, Y. J., Chen, T., Romero, B. A., Wang, Y., Deng, J., Zhang, T., Crabtree, G. R., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c17396 · Cited by 3 · see citing works

Native mass spectrometry for proximity-inducing compounds: a new opportunity for studying chemical-induced protein modulation

Fabbrizi, E., Fiorentino, F., Casano, F., Mai, A., & Rotili, D. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2486146 · Cited by 3 · see citing works

Benchmarking of PROTAC docking and virtual screening toolsPreprint

Rovers, E., & Schapira, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.30.555318 · Cited by 3 · see citing works

Rewiring DNA repair with PARP-based chemical inducers of proximityPreprint

da Camara, B., Bilotta, E. M., Broderick, E., Premashankar, A., Barta, P. A., Carter, T. R., Hargis, L. M., Durocher, D., & Erb, M. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.26.666954 · Cited by 3 · see citing works

Induced proximity for dephosphorylation

Park, K.-S., & Kwon, T. K. (2026) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2026.02.010 · Cited by 2 · see citing works

Proximity-Induced Phosphatase-Recruiting DNA Feedback Switch for Self-Adaptive Modulation of Receptor Signaling and Cell Behavior

Wu, Y., Yin, G., Zhang, Q., Qi, L., Zhang, B., Chen, M., Liu, L., Zhou, Y., He, L., Wang, H.-H., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c05492 · Cited by 2 · see citing works

Molecular glues and PROTACs: unlocking targeted protein degradation in plant biology

Donderis-Fagoaga, C., Orea-Ordóñez, L., & Lozano‐Juste, J. (2026) · Journal of Experimental Botany · doi:10.1093/jxb/erag256 · Cited by 2 · see citing works

Modulating phosphorylation by proximity-inducing strategy: an update

Xia, Y., Zhai, D., You, Q., Wang, L., & Zhang, Q. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00484a · Cited by 2 · see citing works

Advances in AR-Targeting Chimeras: A Case Study of proteolysis-targeting Chimeras From Bench to Bedside

Du, W. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2022-0147 · Cited by 2 · see citing works

Cellular Principles of Targeted Protein Degradation

Diamantino, J., & Hellerschmied, D. (2022) · Wiley eBooks · doi:10.1002/9783527836208.ch2 · Cited by 2 · see citing works

Sculpting Cell Fate: The Expanding Universe of Nondegradative Proximity‐Inducing Tools

Xiao, H., Wang, L., Chen, M., Zhen, T., Chen, Y., & Sun, H. (2026) · ChemMedChem · doi:10.1002/cmdc.202501088 · Cited by 1 · see citing works

FoxO signaling in regulated cell death and its therapeutic implications in inflammation

Zhang, K., Mo, C., Wen, B., Ma, Z., & Ma, D. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116830 · Cited by 1 · see citing works

Heterobifunctional molecules tackle targeted protein dephosphorylation

Sibley, C. D., & Schneekloth, J. S. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.01.005 · Cited by 8 · see citing works

TogoPhosTAC: A Ready-To-Go and Adaptable Targeted Protein Dephosphorylation SystemPreprint

Chen, P., Chen, Y.-Y., Ke, D.-T., Lee, Y., Yeh, C.-L., Ko, Y.-C., Tu, M., Yu, C., & Hu, Z. (2025) · Research Square · doi:10.21203/rs.3.rs-6126609/v1

Deciphering phosphorylation TACtics: Advances in phosphorylation targeting strategies and bifunctional modalities

Ke, D.-T., Zhan, Z., Zhang, W., Hu, Z., & Chen, P. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2025.12.012 · Cited by 7 · see citing works

Rewriting Phosphorylation Codes: Toward Signal-State Editing with PhosTACs

Ke, D.-T., Chang, W.-C., Chen, Y.-Y., & Chen, P. (2026) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases4040029

Posttranslational protein knockdown coupled to receptor tyrosine kinase activation with phosphoPROTACs

Hines, J. F., Gough, J. D., Corson, T. W., & Crews, C. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217206110 · Cited by 177 · see citing works